3PASE_NITEU
ID 3PASE_NITEU Reviewed; 151 AA.
AC Q82UI9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Inorganic triphosphatase;
DE Short=PPPase;
DE EC=3.6.1.25;
GN OrderedLocusNames=NE1496;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RA Lunin V.V., Skarina T., Onopriyenko O., Binkowski T.A., Joachimiak A.,
RA Edwards A.M., Savchenko A.;
RT "The crystal structure of the hypothetical protein NE1496.";
RL Submitted (DEC-2005) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF LYS-7; TYR-27; LYS-51 AND LYS-84, ACTIVE SITE,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, REACTION MECHANISM,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=21840996; DOI=10.1074/jbc.m111.233585;
RA Delvaux D., Murty M.R., Gabelica V., Lakaye B., Lunin V.V., Skarina T.,
RA Onopriyenko O., Kohn G., Wins P., De Pauw E., Bettendorff L.;
RT "A specific inorganic triphosphatase from Nitrosomonas europaea: structure
RT and catalytic mechanism.";
RL J. Biol. Chem. 286:34023-34035(2011).
CC -!- FUNCTION: Involved in the hydrolysis of the beta-gamma-phosphoanhydride
CC linkage of triphosphate-containing substrates (inorganic or nucleoside-
CC linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The
CC enzyme has a strong preference for linear PPPi compared with cyclic
CC PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains
CC polyphosphate are not hydrolyzed. It has only a slight thiamine
CC triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity
CC is negligible in the presence of magnesium, but a small activity is
CC observed in the presence of manganese, in particular with GTP.
CC {ECO:0000269|PubMed:21840996}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + triphosphate = diphosphate + phosphate;
CC Xref=Rhea:RHEA:14157, ChEBI:CHEBI:15377, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.25;
CC Evidence={ECO:0000269|PubMed:21840996};
CC -!- ACTIVITY REGULATION: Activated by magnesium and mangenese ions, and
CC inhibited by calcium, zinc and copper ions.
CC {ECO:0000269|PubMed:21840996}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for PPPi (at pH 9.7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21840996};
CC KM=40 uM for PPPi (at pH 9.7 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:21840996};
CC KM=58 uM for PPPi (at pH 7.1 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:21840996};
CC KM=800 uM for ATP (at pH 8.1 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:21840996};
CC Vmax=910 umol/min/mg enzyme with PPPi as substrate (at pH 9.7 and 50
CC degrees Celsius) {ECO:0000269|PubMed:21840996};
CC Vmax=240 umol/min/mg enzyme with PPPi as substrate (at pH 9.7 and 37
CC degrees Celsius) {ECO:0000269|PubMed:21840996};
CC Vmax=60 umol/min/mg enzyme with PPPi as substrate (at pH 7.1 and 37
CC degrees Celsius) {ECO:0000269|PubMed:21840996};
CC Vmax=1.2 umol/min/mg enzyme with ATP as substrate (at pH 8.1 and 50
CC degrees Celsius) {ECO:0000269|PubMed:21840996};
CC Note=kcat is 288 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 50
CC degrees Celsius). kcat is 76 sec(-1) for hydrolysis of PPPi (at pH
CC 9.7 and 37 degrees Celsius). kcat is 19 sec(-1) for hydrolysis of
CC PPPi (at pH 7.1 and 37 degrees Celsius). kcat is 0.36 sec(-1) for
CC hydrolysis of ATP (at pH 8.1 and 50 degrees Celsius).;
CC pH dependence:
CC Optimum pH is around 9.7. {ECO:0000269|PubMed:21840996};
CC Temperature dependence:
CC Optimum temperature is between 50 and 55 degrees Celsius.
CC {ECO:0000269|PubMed:21840996};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21840996}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL954747; CAD85407.1; -; Genomic_DNA.
DR RefSeq; WP_011112064.1; NC_004757.1.
DR PDB; 2FBL; X-ray; 1.90 A; A/B=1-151.
DR PDB; 3TYP; X-ray; 1.90 A; A/B=2-151.
DR PDBsum; 2FBL; -.
DR PDBsum; 3TYP; -.
DR AlphaFoldDB; Q82UI9; -.
DR SMR; Q82UI9; -.
DR STRING; 228410.NE1496; -.
DR EnsemblBacteria; CAD85407; CAD85407; NE1496.
DR KEGG; neu:NE1496; -.
DR eggNOG; COG2954; Bacteria.
DR HOGENOM; CLU_109545_0_0_4; -.
DR OMA; SINEFCY; -.
DR OrthoDB; 1469073at2; -.
DR PhylomeDB; Q82UI9; -.
DR EvolutionaryTrace; Q82UI9; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0050355; F:triphosphatase activity; IDA:UniProtKB.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR012042; NeuTTM/CthTTM-like.
DR PANTHER; PTHR40114; PTHR40114; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF016487; CYTH_UCP016487; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..151
FT /note="Inorganic triphosphatase"
FT /id="PRO_0000426735"
FT DOMAIN 1..148
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21840996"
FT MUTAGEN 7
FT /note="K->A: No effect on hydrolase activity."
FT /evidence="ECO:0000269|PubMed:21840996"
FT MUTAGEN 27
FT /note="Y->F: Strong loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:21840996"
FT MUTAGEN 51
FT /note="K->R: The affinity is strongly decreased and the
FT catalytic efficiency is at least 1000 times lower than that
FT of the wild-type. Manganese ions do not induce a
FT significant activation."
FT /evidence="ECO:0000269|PubMed:21840996"
FT MUTAGEN 84
FT /note="K->A: It is 10 times less active than the wild-type
FT and the affinity for PPPi is 2 orders of magnitude lower
FT than for the wild-type. Mutant is more strongly activated
FT by manganese ions than by magnesium ions, and the
FT inhibitory effects of calcium and zinc ions are less
FT pronounced."
FT /evidence="ECO:0000269|PubMed:21840996"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2FBL"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:2FBL"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2FBL"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:2FBL"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:2FBL"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2FBL"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2FBL"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:2FBL"
SQ SEQUENCE 151 AA; 17314 MW; B5A584857833ECCA CRC64;
MTEIERKFLV ATFPDGELHA VPLRQGYLTT PTDSIELRLR QQGTEYFMTL KSEGGLSRQE
YEIQIDVTQF EMLWPATEGR RVEKTRYSGK LPDGQLFELD VFAGHLSPLM LVEVEFLSED
AAQAFIPPPW FGEEVTEDKR YKNKALALSI P
